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NameN(G),N(G)-dimethylarginine dimethylaminohydrolase 1
Synonyms
  • 3.5.3.18
  • DDAH
  • DDAH-1
  • DDAHI
  • Dimethylargininase-1
Gene NameDDAH1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037071|N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGL
QVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMK
DENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSM
AGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPE
EYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
Number of residues285
Molecular Weight31121.5
Theoretical pI5.61
GO Classification
Functions
  • amino acid binding
  • metal ion binding
  • dimethylargininase activity
  • catalytic activity
Processes
  • small molecule metabolic process
  • positive regulation of angiogenesis
  • arginine catabolic process
  • nitric oxide mediated signal transduction
  • nitric oxide metabolic process
  • regulation of nitric-oxide synthase activity
  • positive regulation of nitric oxide biosynthetic process
  • regulation of systemic arterial blood pressure
  • citrulline metabolic process
Components
  • cytosol
  • extracellular exosome
  • mitochondrion
General FunctionMetal ion binding
Specific FunctionHydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID4160666
UniProtKB IDO94760
UniProtKB Entry NameDDAH1_HUMAN
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0021273|N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH1)
ATGATGAAAGAAGCATTAGAAAAACTTCAGCTCAATATAGTAGAGATGAAAGATGAAAAT
GCAACTTTAGATGGCGGAGATGTTTTATTCACAGGCAGAGAATTTTTTGTGGGCCTTTCC
AAAAGGACAAATCAACGAGGTGCTGAAATCTTGGCTGATACTTTTAAGGACTATGCAGTC
TCCACAGTGCCAGTGGCAGATGGGTTGCATTTGAAGAGTTTCTGCAGCATGGCTGGGCCT
AACCTGATCGCAATTGGGTCTAGTGAATCTGCACAGAAGGCCCTTAAGATCATGCAACAG
ATGAGTGACCACCGCTACGACAAACTCACTGTGCCTGATGACATAGCAGCAAACTGTATA
TATCTAAATATCCCCAACAAAGGGCACGTCTTGCTGCACCGAACCCCGGAAGAGTATCCA
GAAAGTGCAAAGGTTTATGAGAAACTGAAGGACCATATGCTGATCCCCGTGAGCATGTCT
GAACTGGAAAAGGTGGATGGGCTGCTCACCTGCTGCTCAGTTTTAATTAACAAGAAAGTA
GACTCCTGA
GenBank Gene IDAB001915
GeneCard IDNot Available
GenAtlas IDDDAH1
HGNC IDHGNC:2715
Chromosome Location1
Locus1p22
References
  1. Kimoto M, Miyatake S, Sasagawa T, Yamashita H, Okita M, Oka T, Ogawa T, Tsuji H: Purification, cDNA cloning and expression of human NG,NG-dimethylarginine dimethylaminohydrolase. Eur J Biochem. 1998 Dec 1;258(2):863-8. 9874257
  2. Leiper JM, Santa Maria J, Chubb A, MacAllister RJ, Charles IG, Whitley GS, Vallance P: Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochem J. 1999 Oct 1;343 Pt 1:209-14. 10493931
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. 17974005
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  6. Forbes SP, Druhan LJ, Guzman JE, Parinandi N, Zhang L, Green-Church KB, Cardounel AJ: Mechanism of 4-HNE mediated inhibition of hDDAH-1: implications in no regulation. Biochemistry. 2008 Feb 12;47(6):1819-26. doi: 10.1021/bi701659n. Epub 2008 Jan 3. 18171027
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  11. Wang Y, Monzingo AF, Hu S, Schaller TH, Robertus JD, Fast W: Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide. Biochemistry. 2009 Sep 15;48(36):8624-35. doi: 10.1021/bi9007098. 19663506